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Volumn 1860, Issue 8, 2016, Pages 1795-1808

Glycomic analysis of gastric carcinoma cells discloses glycans as modulators of RON receptor tyrosine kinase activation in cancer

Author keywords

Gastric cancer; Glycome; RON; Sialome; Sialyl Lewis X (SLeX); ST3GAL4

Indexed keywords

GLYCAN DERIVATIVE; PROTEIN TYROSINE KINASE; RON RECEPTOR TYROSINE KINASE; SIALYLTRANSFERASE; SIALYLTRANSFERASE ST3GAL4; UNCLASSIFIED DRUG; BETA-GALACTOSIDE ALPHA-2,3-SIALYLTRANSFERASE; CD15 ANTIGEN; POLYSACCHARIDE; RON PROTEIN; SIALYL LEWIS X ANTIGEN; TUMOR PROTEIN;

EID: 84952685671     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2015.12.016     Document Type: Article
Times cited : (46)

References (80)
  • 2
    • 84903754348 scopus 로고    scopus 로고
    • Statistics: Attacking an epidemic
    • M. May Statistics: attacking an epidemic Nature 509 2014 S50 S51
    • (2014) Nature , vol.509 , pp. S50-S51
    • May, M.1
  • 5
    • 77950410995 scopus 로고    scopus 로고
    • Alterations in glycosylation as biomarkers for cancer detection
    • C.A. Reis, H. Osorio, L. Silva, C. Gomes, and L. David Alterations in glycosylation as biomarkers for cancer detection J. Clin. Pathol. 63 2010 322 329
    • (2010) J. Clin. Pathol. , vol.63 , pp. 322-329
    • Reis, C.A.1    Osorio, H.2    Silva, L.3    Gomes, C.4    David, L.5
  • 6
    • 67649847234 scopus 로고    scopus 로고
    • Glycosylation Changes in Cancer
    • A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, Cold Spring Harbor NY
    • A. Varki, R. Kannagi, and B.P. Toole Glycosylation Changes in Cancer A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, Essentials of Glycobiology 2009 Cold Spring Harbor NY
    • (2009) Essentials of Glycobiology
    • Varki, A.1    Kannagi, R.2    Toole, B.P.3
  • 7
    • 84940449986 scopus 로고    scopus 로고
    • Glycosylation in cancer: Mechanisms and clinical implications
    • S.S. Pinho, and C.A. Reis Glycosylation in cancer: mechanisms and clinical implications Nat. Rev. Cancer 15 2015 540 555
    • (2015) Nat. Rev. Cancer , vol.15 , pp. 540-555
    • Pinho, S.S.1    Reis, C.A.2
  • 9
    • 77951778977 scopus 로고    scopus 로고
    • Personalized medicine in oncology: The future is now
    • R.L. Schilsky Personalized medicine in oncology: the future is now Nat. Rev. Drug Discov. 9 2010 363 366
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 363-366
    • Schilsky, R.L.1
  • 10
    • 9244222261 scopus 로고    scopus 로고
    • Targeted cancer therapy
    • C. Sawyers Targeted cancer therapy Nature 432 2004 294 297
    • (2004) Nature , vol.432 , pp. 294-297
    • Sawyers, C.1
  • 11
    • 27544479318 scopus 로고    scopus 로고
    • Role of tyrosine kinase inhibitors in cancer therapy
    • A. Arora, and E.M. Scholar Role of tyrosine kinase inhibitors in cancer therapy J. Pharmacol. Exp. Ther. 315 2005 971 979
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 971-979
    • Arora, A.1    Scholar, E.M.2
  • 12
    • 84881089423 scopus 로고    scopus 로고
    • MSP-RON signalling in cancer: Pathogenesis and therapeutic potential
    • H.P. Yao, Y.Q. Zhou, R. Zhang, and M.H. Wang MSP-RON signalling in cancer: pathogenesis and therapeutic potential Nat. Rev. Cancer 13 2013 466 481
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 466-481
    • Yao, H.P.1    Zhou, Y.Q.2    Zhang, R.3    Wang, M.H.4
  • 13
    • 70649087034 scopus 로고    scopus 로고
    • Differential expression of alpha-2,3-sialyltransferases and alpha-1,3/4-fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells
    • A.S. Carvalho, A. Harduin-Lepers, A. Magalhaes, E. Machado, N. Mendes, L.T. Costa, R. Matthiesen, R. Almeida, J. Costa, and C.A. Reis Differential expression of alpha-2,3-sialyltransferases and alpha-1,3/4-fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells Int. J. Biochem. Cell Biol. 42 2010 80 89
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 80-89
    • Carvalho, A.S.1    Harduin-Lepers, A.2    Magalhaes, A.3    Machado, E.4    Mendes, N.5    Costa, L.T.6    Matthiesen, R.7    Almeida, R.8    Costa, J.9    Reis, C.A.10
  • 14
    • 77649216263 scopus 로고    scopus 로고
    • MUC2 mucin is a major carrier of the cancer-associated sialyl-Tn antigen in intestinal metaplasia and gastric carcinomas
    • T. Conze, A.S. Carvalho, U. Landegren, R. Almeida, C.A. Reis, L. David, and O. Soderberg MUC2 mucin is a major carrier of the cancer-associated sialyl-Tn antigen in intestinal metaplasia and gastric carcinomas Glycobiology 20 2010 199 206
    • (2010) Glycobiology , vol.20 , pp. 199-206
    • Conze, T.1    Carvalho, A.S.2    Landegren, U.3    Almeida, R.4    Reis, C.A.5    David, L.6    Soderberg, O.7
  • 15
    • 12644292106 scopus 로고
    • The two histological main types of gastric carcinoma: Diffuse and so-called intestinal-type carcinoma. An attempt at a histo-clinical classification
    • P. Lauren The two histological main types of gastric carcinoma: diffuse and so-called intestinal-type carcinoma. An attempt at a histo-clinical classification Acta Pathol. Microbiol. Scand. 64 1965 31 49
    • (1965) Acta Pathol. Microbiol. Scand. , vol.64 , pp. 31-49
    • Lauren, P.1
  • 16
    • 0036894272 scopus 로고    scopus 로고
    • Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis
    • B.L. Schulz, N.H. Packer, and N.G. Karlsson Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis Anal. Chem. 74 2002 6088 6097
    • (2002) Anal. Chem. , vol.74 , pp. 6088-6097
    • Schulz, B.L.1    Packer, N.H.2    Karlsson, N.G.3
  • 17
    • 34447310112 scopus 로고    scopus 로고
    • Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions
    • L. Royle, C.M. Radcliffe, R.A. Dwek, and P.M. Rudd Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions Methods Mol. Biol. 347 2006 125 143
    • (2006) Methods Mol. Biol. , vol.347 , pp. 125-143
    • Royle, L.1    Radcliffe, C.M.2    Dwek, R.A.3    Rudd, P.M.4
  • 19
    • 84964211695 scopus 로고    scopus 로고
    • Comprehensive protocol to simultaneously study protein phosphorylation, acetylation, and N-linked sialylated glycosylation
    • M.N. Melo-Braga, M. Ibanez-Vea, M.R. Larsen, and K. Kulej Comprehensive protocol to simultaneously study protein phosphorylation, acetylation, and N-linked sialylated glycosylation Methods Mol. Biol. 1295 2015 275 292
    • (2015) Methods Mol. Biol. , vol.1295 , pp. 275-292
    • Melo-Braga, M.N.1    Ibanez-Vea, M.2    Larsen, M.R.3    Kulej, K.4
  • 20
    • 84883805454 scopus 로고    scopus 로고
    • Assessment and improvement of statistical tools for comparative proteomics analysis of sparse data sets with few experimental replicates
    • V. Schwammle, I.R. Leon, and O.N. Jensen Assessment and improvement of statistical tools for comparative proteomics analysis of sparse data sets with few experimental replicates J. Proteome Res. 12 2013 3874 3883
    • (2013) J. Proteome Res. , vol.12 , pp. 3874-3883
    • Schwammle, V.1    Leon, I.R.2    Jensen, O.N.3
  • 22
    • 0027379674 scopus 로고
    • Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection
    • K. Sasaki, E. Watanabe, K. Kawashima, S. Sekine, T. Dohi, M. Oshima, N. Hanai, T. Nishi, and M. Hasegawa Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection J. Biol. Chem. 268 1993 22782 22787
    • (1993) J. Biol. Chem. , vol.268 , pp. 22782-22787
    • Sasaki, K.1    Watanabe, E.2    Kawashima, K.3    Sekine, S.4    Dohi, T.5    Oshima, M.6    Hanai, N.7    Nishi, T.8    Hasegawa, M.9
  • 23
    • 0028174078 scopus 로고
    • Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups
    • H. Kitagawa, and J.C. Paulson Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups J. Biol. Chem. 269 1994 1394 1401
    • (1994) J. Biol. Chem. , vol.269 , pp. 1394-1401
    • Kitagawa, H.1    Paulson, J.C.2
  • 24
    • 84879165131 scopus 로고    scopus 로고
    • Expression of ST3GAL4 leads to SLe(x) expression and induces c-Met activation and an invasive phenotype in gastric carcinoma cells
    • C. Gomes, H. Osorio, M.T. Pinto, D. Campos, M.J. Oliveira, and C.A. Reis Expression of ST3GAL4 leads to SLe(x) expression and induces c-Met activation and an invasive phenotype in gastric carcinoma cells PLoS One 8 2013 e66737
    • (2013) PLoS One , vol.8
    • Gomes, C.1    Osorio, H.2    Pinto, M.T.3    Campos, D.4    Oliveira, M.J.5    Reis, C.A.6
  • 31
    • 33746504571 scopus 로고    scopus 로고
    • Invasive growth: A MET-driven genetic programme for cancer and stem cells
    • C. Boccaccio, and P.M. Comoglio Invasive growth: a MET-driven genetic programme for cancer and stem cells Nat. Rev. Cancer 6 2006 637 645
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 637-645
    • Boccaccio, C.1    Comoglio, P.M.2
  • 32
    • 84890442740 scopus 로고    scopus 로고
    • Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) in cancer progression and metastasis
    • N. Beauchemin, and A. Arabzadeh Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) in cancer progression and metastasis Cancer Metastasis Rev. 32 2013 643 671
    • (2013) Cancer Metastasis Rev. , vol.32 , pp. 643-671
    • Beauchemin, N.1    Arabzadeh, A.2
  • 33
    • 72949119124 scopus 로고    scopus 로고
    • Integrins in cancer: Biological implications and therapeutic opportunities
    • J.S. Desgrosellier, and D.A. Cheresh Integrins in cancer: biological implications and therapeutic opportunities Nat. Rev. Cancer 10 2010 9 22
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 9-22
    • Desgrosellier, J.S.1    Cheresh, D.A.2
  • 34
    • 36749041486 scopus 로고    scopus 로고
    • Altered expression of the RON receptor tyrosine kinase in various epithelial cancers and its contribution to tumourigenic phenotypes in thyroid cancer cells
    • M.H. Wang, W. Lee, Y.L. Luo, M.T. Weis, and H.P. Yao Altered expression of the RON receptor tyrosine kinase in various epithelial cancers and its contribution to tumourigenic phenotypes in thyroid cancer cells J. Pathol. 213 2007 402 411
    • (2007) J. Pathol. , vol.213 , pp. 402-411
    • Wang, M.H.1    Lee, W.2    Luo, Y.L.3    Weis, M.T.4    Yao, H.P.5
  • 35
    • 74449090319 scopus 로고    scopus 로고
    • The Ron receptor tyrosine kinase positively regulates angiogenic chemokine production in prostate cancer cells
    • M.N. Thobe, D. Gurusamy, P. Pathrose, and S.E. Waltz The Ron receptor tyrosine kinase positively regulates angiogenic chemokine production in prostate cancer cells Oncogene 29 2010 214 226
    • (2010) Oncogene , vol.29 , pp. 214-226
    • Thobe, M.N.1    Gurusamy, D.2    Pathrose, P.3    Waltz, S.E.4
  • 37
    • 77956039906 scopus 로고    scopus 로고
    • Ron receptor tyrosine kinase activation confers resistance to tamoxifen in breast cancer cell lines
    • R.J. McClaine, A.M. Marshall, P.K. Wagh, and S.E. Waltz Ron receptor tyrosine kinase activation confers resistance to tamoxifen in breast cancer cell lines Neoplasia 12 2010 650 658
    • (2010) Neoplasia , vol.12 , pp. 650-658
    • McClaine, R.J.1    Marshall, A.M.2    Wagh, P.K.3    Waltz, S.E.4
  • 39
    • 0029837671 scopus 로고    scopus 로고
    • A splicing variant of the RON transcript induces constitutive tyrosine kinase activity and an invasive phenotype
    • C. Collesi, M.M. Santoro, G. Gaudino, and P.M. Comoglio A splicing variant of the RON transcript induces constitutive tyrosine kinase activity and an invasive phenotype Mol. Cell. Biol. 16 1996 5518 5526
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5518-5526
    • Collesi, C.1    Santoro, M.M.2    Gaudino, G.3    Comoglio, P.M.4
  • 40
    • 0029997180 scopus 로고    scopus 로고
    • Constitutive activation of the RON gene promotes invasive growth but not transformation
    • M.M. Santoro, C. Collesi, S. Grisendi, G. Gaudino, and P.M. Comoglio Constitutive activation of the RON gene promotes invasive growth but not transformation Mol. Cell. Biol. 16 1996 7072 7083
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7072-7083
    • Santoro, M.M.1    Collesi, C.2    Grisendi, S.3    Gaudino, G.4    Comoglio, P.M.5
  • 41
    • 0031937018 scopus 로고    scopus 로고
    • Dimeric sialyl-Le(x) expression in gastric carcinoma correlates with venous invasion and poor outcome
    • M. Amado, F. Carneiro, M. Seixas, H. Clausen, and M. Sobrinho-Simoes Dimeric sialyl-Le(x) expression in gastric carcinoma correlates with venous invasion and poor outcome Gastroenterology 114 1998 462 470
    • (1998) Gastroenterology , vol.114 , pp. 462-470
    • Amado, M.1    Carneiro, F.2    Seixas, M.3    Clausen, H.4    Sobrinho-Simoes, M.5
  • 42
    • 0030811894 scopus 로고    scopus 로고
    • Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer
    • R. Kannagi Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer Glycoconj. J. 14 1997 577 584
    • (1997) Glycoconj. J. , vol.14 , pp. 577-584
    • Kannagi, R.1
  • 44
    • 0032418052 scopus 로고    scopus 로고
    • Immunohistochemical expression of the sialyl Lewis x antigen on gastric cancer cells correlates with the presence of liver metastasis
    • M. Tatsumi, A. Watanabe, H. Sawada, Y. Yamada, Y. Shino, and H. Nakano Immunohistochemical expression of the sialyl Lewis x antigen on gastric cancer cells correlates with the presence of liver metastasis Clin. Exp. Metastasis 16 1998 743 750
    • (1998) Clin. Exp. Metastasis , vol.16 , pp. 743-750
    • Tatsumi, M.1    Watanabe, A.2    Sawada, H.3    Yamada, Y.4    Shino, Y.5    Nakano, H.6
  • 45
    • 7844240122 scopus 로고    scopus 로고
    • Histopathological subtypes and prognosis of gastric cancer are correlated with the expression of mucin-associated sialylated antigens: Sialosyl-Lewis(a), sialosyl-Lewis(x) and sialosyl-Tn
    • S.E. Baldus, T.K. Zirbes, S.P. Monig, S. Engel, E. Monaca, K. Rafiqpoor, F.G. Hanisch, C. Hanski, J. Thiele, H. Pichlmaier, and H.P. Dienes Histopathological subtypes and prognosis of gastric cancer are correlated with the expression of mucin-associated sialylated antigens: sialosyl-Lewis(a), sialosyl-Lewis(x) and sialosyl-Tn Tumour Biol. 19 1998 445 453
    • (1998) Tumour Biol. , vol.19 , pp. 445-453
    • Baldus, S.E.1    Zirbes, T.K.2    Monig, S.P.3    Engel, S.4    Monaca, E.5    Rafiqpoor, K.6    Hanisch, F.G.7    Hanski, C.8    Thiele, J.9    Pichlmaier, H.10    Dienes, H.P.11
  • 47
    • 0030745147 scopus 로고    scopus 로고
    • Perspectives on the significance of altered glycosylation of glycoproteins in cancer
    • Y.J. Kim, and A. Varki Perspectives on the significance of altered glycosylation of glycoproteins in cancer Glycoconj. J. 14 1997 569 576
    • (1997) Glycoconj. J. , vol.14 , pp. 569-576
    • Kim, Y.J.1    Varki, A.2
  • 48
    • 0035526267 scopus 로고    scopus 로고
    • Sialyltransferases in cancer
    • F. Dall'Olio, and M. Chiricolo Sialyltransferases in cancer Glycoconj. J. 18 2001 841 850
    • (2001) Glycoconj. J. , vol.18 , pp. 841-850
    • Dall'Olio, F.1    Chiricolo, M.2
  • 49
    • 0036351383 scopus 로고    scopus 로고
    • Cell surface alpha 2,6 sialylation affects adhesion of breast carcinoma cells
    • S. Lin, W. Kemmner, S. Grigull, and P.M. Schlag Cell surface alpha 2,6 sialylation affects adhesion of breast carcinoma cells Exp. Cell Res. 276 2002 101 110
    • (2002) Exp. Cell Res. , vol.276 , pp. 101-110
    • Lin, S.1    Kemmner, W.2    Grigull, S.3    Schlag, P.M.4
  • 50
    • 0035883156 scopus 로고    scopus 로고
    • Alpha2,6-sialylation of cell-surface N-glycans inhibits glioma formation in vivo
    • H. Yamamoto, A. Oviedo, C. Sweeley, T. Saito, and J.R. Moskal Alpha2,6-sialylation of cell-surface N-glycans inhibits glioma formation in vivo Cancer Res. 61 2001 6822 6829
    • (2001) Cancer Res. , vol.61 , pp. 6822-6829
    • Yamamoto, H.1    Oviedo, A.2    Sweeley, C.3    Saito, T.4    Moskal, J.R.5
  • 51
    • 31144475414 scopus 로고    scopus 로고
    • Phenotypic changes induced by expression of beta-galactoside alpha2,6 sialyltransferase i in the human colon cancer cell line SW948
    • M. Chiricolo, N. Malagolini, S. Bonfiglioli, and F. Dall'Olio Phenotypic changes induced by expression of beta-galactoside alpha2,6 sialyltransferase I in the human colon cancer cell line SW948 Glycobiology 16 2006 146 154
    • (2006) Glycobiology , vol.16 , pp. 146-154
    • Chiricolo, M.1    Malagolini, N.2    Bonfiglioli, S.3    Dall'Olio, F.4
  • 52
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • R. Kornfeld, and S. Kornfeld Assembly of asparagine-linked oligosaccharides Annu. Rev. Biochem. 54 1985 631 664
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 53
    • 0029618008 scopus 로고
    • Recent progress in the molecular biology of the cloned N-acetylglucosaminyltransferases
    • N. Taniguchi, and Y. Ihara Recent progress in the molecular biology of the cloned N-acetylglucosaminyltransferases Glycoconj. J. 12 1995 733 738
    • (1995) Glycoconj. J. , vol.12 , pp. 733-738
    • Taniguchi, N.1    Ihara, Y.2
  • 54
    • 0037051978 scopus 로고    scopus 로고
    • Abnormal glycosylation and altered Golgi structure in colorectal cancer: Dependence on intra-Golgi pH
    • S. Kellokumpu, R. Sormunen, and I. Kellokumpu Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH FEBS Lett. 516 2002 217 224
    • (2002) FEBS Lett. , vol.516 , pp. 217-224
    • Kellokumpu, S.1    Sormunen, R.2    Kellokumpu, I.3
  • 55
    • 77951072143 scopus 로고    scopus 로고
    • The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression
    • Y. Song, J.A. Aglipay, J.D. Bernstein, S. Goswami, and P. Stanley The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression Cancer Res. 70 2010 3361 3371
    • (2010) Cancer Res. , vol.70 , pp. 3361-3371
    • Song, Y.1    Aglipay, J.A.2    Bernstein, J.D.3    Goswami, S.4    Stanley, P.5
  • 56
    • 84858138360 scopus 로고    scopus 로고
    • Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions
    • S.S. Pinho, P. Oliveira, J. Cabral, S. Carvalho, D. Huntsman, F. Gartner, R. Seruca, C.A. Reis, and C. Oliveira Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions PLoS One 7 2012 e33191
    • (2012) PLoS One , vol.7
    • Pinho, S.S.1    Oliveira, P.2    Cabral, J.3    Carvalho, S.4    Huntsman, D.5    Gartner, F.6    Seruca, R.7    Reis, C.A.8    Oliveira, C.9
  • 57
    • 0024585483 scopus 로고
    • Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens
    • S. Hakomori Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens Adv. Cancer Res. 52 1989 257 331
    • (1989) Adv. Cancer Res. , vol.52 , pp. 257-331
    • Hakomori, S.1
  • 58
    • 84862168794 scopus 로고    scopus 로고
    • Structural analysis of N- and O-glycans released from glycoproteins
    • P.H. Jensen, N.G. Karlsson, D. Kolarich, and N.H. Packer Structural analysis of N- and O-glycans released from glycoproteins Nat. Protoc. 7 2012 1299 1310
    • (2012) Nat. Protoc. , vol.7 , pp. 1299-1310
    • Jensen, P.H.1    Karlsson, N.G.2    Kolarich, D.3    Packer, N.H.4
  • 59
    • 84935870683 scopus 로고    scopus 로고
    • Isomer-specific analysis of released N-glycans by LC-ESI MS/MS with porous graphitized carbon
    • D. Kolarich, M. Windwarder, K. Alagesan, and F. Altmann Isomer-specific analysis of released N-glycans by LC-ESI MS/MS with porous graphitized carbon Methods Mol. Biol. 1321 2015 427 435
    • (2015) Methods Mol. Biol. , vol.1321 , pp. 427-435
    • Kolarich, D.1    Windwarder, M.2    Alagesan, K.3    Altmann, F.4
  • 60
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: Implications for cancer cell biology
    • C. Slawson, and G.W. Hart O-GlcNAc signalling: implications for cancer cell biology Nat. Rev. Cancer 11 2011 678 684
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 63
    • 84878225772 scopus 로고    scopus 로고
    • Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-kappaB activity in pancreatic cancer cells
    • Z. Ma, D.J. Vocadlo, and K. Vosseller Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-kappaB activity in pancreatic cancer cells J. Biol. Chem. 288 2013 15121 15130
    • (2013) J. Biol. Chem. , vol.288 , pp. 15121-15130
    • Ma, Z.1    Vocadlo, D.J.2    Vosseller, K.3
  • 65
    • 5444266511 scopus 로고    scopus 로고
    • Regulation of integrin functions by N-glycans
    • J. Gu, and N. Taniguchi Regulation of integrin functions by N-glycans Glycoconj. J. 21 2004 9 15
    • (2004) Glycoconj. J. , vol.21 , pp. 9-15
    • Gu, J.1    Taniguchi, N.2
  • 66
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • D. Hanahan, and R.A. Weinberg Hallmarks of cancer: the next generation Cell 144 2011 646 674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 72
    • 84877679367 scopus 로고    scopus 로고
    • Small-molecule inhibitor BMS-777607 induces breast cancer cell polyploidy with increased resistance to cytotoxic chemotherapy agents
    • S. Sharma, J.Y. Zeng, C.M. Zhuang, Y.Q. Zhou, H.P. Yao, X. Hu, R. Zhang, and M.H. Wang Small-molecule inhibitor BMS-777607 induces breast cancer cell polyploidy with increased resistance to cytotoxic chemotherapy agents Mol. Cancer Ther. 12 2013 725 736
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 725-736
    • Sharma, S.1    Zeng, J.Y.2    Zhuang, C.M.3    Zhou, Y.Q.4    Yao, H.P.5    Hu, X.6    Zhang, R.7    Wang, M.H.8
  • 77
    • 78649378720 scopus 로고    scopus 로고
    • Deletion or insertion in the first immunoglobulin-plexin-transcription (IPT) domain differentially regulates expression and tumorigenic activities of RON receptor tyrosine kinase
    • Q. Ma, K. Zhang, S. Guin, Y.Q. Zhou, and M.H. Wang Deletion or insertion in the first immunoglobulin-plexin-transcription (IPT) domain differentially regulates expression and tumorigenic activities of RON receptor tyrosine kinase Mol. Cancer 9 2010 307
    • (2010) Mol. Cancer , vol.9 , pp. 307
    • Ma, Q.1    Zhang, K.2    Guin, S.3    Zhou, Y.Q.4    Wang, M.H.5
  • 78
    • 84921519978 scopus 로고    scopus 로고
    • Personalized medicine into the next generation
    • M. Ingelman-Sundberg Personalized medicine into the next generation J. Intern. Med. 277 2015 152 154
    • (2015) J. Intern. Med. , vol.277 , pp. 152-154
    • Ingelman-Sundberg, M.1
  • 79
    • 84928590539 scopus 로고    scopus 로고
    • Hurdles on the road to personalized medicine
    • T. Tursz, and R. Bernards Hurdles on the road to personalized medicine Mol. Oncol. 9 2015 935 939
    • (2015) Mol. Oncol. , vol.9 , pp. 935-939
    • Tursz, T.1    Bernards, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.